Abstract
The enzymatic synthesis of conjugates of lysine and aspartic acid with D-glucose was studied. Optimase M-440 showed the very poor regioselectivity in the transesterification of $N{\alpha}$,$N'{\varepsilon}-di-t-Boc-L-Lys-OTFE$ and N-t-Boc-L-Asp-diOTFE with D-glucose. The acylation of glycosidic -OH and primary -OH of D-glucose occurred. However, Optimase M-440 catalyzed only the acylation of primary -OH group in the transesterification of $N{\alpha}$,$N'{\varepsilon}-di-t-Boc-L-Lys-OTFE$ and N-t-Boc-L-Asp-diOTFE with ${\alpha}-$ and ${\beta}-methylglucopyranoside$ in high yields without any other transesterification. Optimase M-440 also discriminated carboxyl groups of N-t-Boc-L-Asp-diOTFE.